Selectivity, binding affinity, and ionization state of matrix metalloproteinase inhibitors

Haizhen A. Zhong, Jack Arbiser, J. Phillip Bowen

Research output: Contribution to journalArticle

7 Scopus citations


This review highlights some recent advances in the design and development of matrix metalloproteinase inhibitors, especially those targeting MMP-2, MMP-9, and MMP-13. Various zinc-binding groups and non-zinc-binding groups are discussed. Interactions between residues in the critical S1' specificity pocket and MMP inhibitors are given special attention. The influence of ionization states of hydroxamates and retrohydroxamates on the docking outcome and the presence of zinc ions in the active site are explored in light of enhancing enrichment factors for docking studies. Details are given to structural factors for the development of more selective and more potent MMP inhibitors.

Original languageEnglish (US)
Pages (from-to)4701-4713
Number of pages13
JournalCurrent Pharmaceutical Design
Issue number26
StatePublished - Aug 15 2013



  • And zinc binding group
  • Cancer
  • Docking
  • MMP-13
  • MMP-2
  • MMP-3
  • Osteoarthritis
  • Rheumatoid arthritis

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

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